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Target Concepts:
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Query: UNIPROT:P17931 (
galectin-3
)
2,860
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
To investigate the involvement of
galectin-3
in the process of neurodegeneration in prion diseases, the expression and cellular localization of
galectin-3
in the brain were studied in scrapie, a mouse model of prion disease. Reverse transcription-polymerase chain reaction (RT-PCR) and Western blot analyses showed that the expression of
galectin-3
protein and mRNA was induced in scrapie-affected brains, particularly at the time when the abnormal prion protein PrP(Sc) began to accumulate in the brains. Immunohistochemically, immunostaining for
galectin-3
was found mainly in B4-isolectin-positive cells (presumably activated microglia/macrophages), but not in astrocytes.
Galectin-3
immunoreactivity was localized mainly in areas of
PrP
(Sc) accumulation and neuronal death in scrapie-infected brains. These findings suggest that the expression of
galectin-3
by activated microglia/macrophages in prion disease correlates with abnormal prion protein accumulation.
...
PMID:Galectin-3 expression is correlated with abnormal prion protein accumulation in murine scrapie. 1753 84
Galectin-3
is a multi-functional protein and participates in mediating inflammatory reactions. The pronounced overexpression of
galectin-3
in prion-infected brain tissue prompted us to study the role of this protein in a murine prion model. Immunofluorescence double-labelling identified microglia as the major cell type expressing
galectin-3
. Ablation of
galectin-3
did not affect
PrP
(Sc)-deposition and development of gliosis. However,
galectin-3
(-/-)-mice showed prolonged survival times upon intracerebral and peripheral scrapie infections. Moreover, protein levels of the lysosomal activation marker LAMP-2 were markedly reduced in prion-infected
galectin-3
(-/-)-mice suggesting a role of
galectin-3
in regulation of lysosomal functions. Lower mRNA levels of Beclin-1 and Atg5 in prion-infected wild-type and
galectin-3
(-/-)-mice indicated an impairment of autophagy although autophagosome formation was unchanged. The results point towards a detrimental role of
galectin-3
in prion infections of the CNS and suggest that endo-/lysosomal dysfunction in combination with reduced autophagy may contribute to disease development.
...
PMID:Role of galectin-3 in prion infections of the CNS. 1755 13
Prion diseases are infectious and fatal neurodegenerative diseases which require the cellular prion protein, PrPC, for development of diseases. The current study shows that the PrPC augments infectivity and plaque formation of a mouse endogenous retrovirus, MuLV. We have established four neuronal cell lines expressing mouse PrPC, PrP+/+; two express wild type PrPC (MoPrPwild) and the other two express mutant PrPC (MoPrPmut). Infection of neuronal cells from various PrP+/+ and
PrP
-/- (MoPrPKO) lines with MuLV yielded at least three times as many plaques in PrP+/+ than in
PrP
-/-. Furthermore, among the four PrP+/+ lines, one mutant line, P101L, had at least 2.5 times as many plaques as the other three PrP+/+ lines. Plaques in P101L were four times larger than those in other PrP+/+ lines. Colocalization of
PrP
and CAgag was seen in MuLV-infected PrP+/+ cells. In the
PrP
-MuLV interaction, the involvement of
galectin-3
and -6 was observed by immunoprecipitation with antibody to PrPC. These results suggest that PrPC combined with
galectin-3
and -6 can act as a receptor for MuLV. P101L, the disease form of mutant PrPC results suggest the genetic mutant form of PrPC may be more susceptible to viral infection.
...
PMID:Cellular Prion Protein Combined with Galectin-3 and -6 Affects the Infectivity Titer of an Endogenous Retrovirus Assayed in Hippocampal Neuronal Cells. 2793 17
